P41597: C-C chemokine receptor type 2 (CCR2)

C-C chemokine receptor type 2 (CCR2) is a 374-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P41597.

Gene
CCR2
Organism
Homo sapiens
Length
374 residues
Mean pLDDT
77.8
Model
AF-P41597-F1 v6
Model created
1 Aug 2025
PDB structures
7

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Model confidence (pLDDT)

The mean pLDDT of this model is 77.8 (confident overall). pLDDT is AlphaFold's per-residue confidence score from 0 to 100. In MolViewer, choose the B-factor color scheme to color the model by pLDDT, because AlphaFold stores it in the B-factor column.

pLDDT bandMeaningShare of residues
Above 90Very high: backbone and side chains are usually accurate53%
70 to 90Confident: backbone generally right19%
50 to 70Low: treat with caution8%
Below 50Very low: often disordered regions21%

What pLDDT means and how to read it

Function

Key functional receptor for CCL2 but can also bind CCL7, and CCL12 (PubMed:23408426, PubMed:38157855, PubMed:8048929, PubMed:8146186). Also transduces signaling mediated by CCL13 (PubMed:38157855). Its binding with CCL2 on monocytes and macrophages mediates chemotaxis and migration induction through the activation of the PI3K cascade, the small G protein Rac and lamellipodium protrusion (PubMed:38157855). Also acts as a receptor for the beta-defensin DEFB106A/DEFB106B (PubMed:23938203). Regulates the expression of T-cell inflammatory cytokines and T-cell differentiation, promoting the differentiation of T-cells into T-helper 17 cells (Th17) during inflammation (By similarity). Facilitates…

Subunit structure

Interacts with ARRB1 (PubMed:9501202). Interacts (via extracellular N-terminal region) with beta-defensin DEFB106A/DEFB106B; this interaction may preferentially require specific tyrosine sulfation on CCR2 (PubMed:23938203). Interacts with NUP85; the interaction is required for CCR2 clusters formation on the cell membrane and CCR2 signaling (PubMed:15995708, PubMed:25283965). Interacts with GNAI1…

Subcellular location

Cell membrane

Disease associations

Experimental structures in the PDB

Compare the prediction with experimentally determined structures of the same protein:

PDB IDMethodResolutionChains and residues
7P8XX-ray1.4 ÅM=25-29
6GPXX-ray2.7 ÅA/B=29-231, A/B=235-321
5T1AX-ray2.81 ÅA=2-318
7XA3EM2.9 ÅR=1-318
6GPSX-ray3.3 ÅA=2-231, A=235-374
2MLONMRA=310-318
2MLQNMRA=310-318

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